Serpin: Difference between revisions

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<StructureSection load='3ndd' size='400' side='right' caption='Structure of cleaved human serpin A1.  Residues 46-382 (grey), residues 383-418 (green). (PDB entry [[3ndd]])' scene=''>
<StructureSection load='2xn6' size='350' side='right' caption='Structure of cleaved human serpin A7.  Residues 32-380 (cyan), residues 381-415 (salmon) complex with thyroxine-fluoresein, ethylene glycol and Ca+2 ion (green) (PDB entry [[2xn6]])' scene='51/517379/Cv/1'>
== Function ==
'''Serpin or serine protease inhibitor''' (Ser) are protease inhibitors.<br />
* Ser C1 is [[Antithrombin]].<br />
* Ser A5 is protein C inhibitor.<br />
* Ser A6 is [[Corticosteroid-binding globulin]]. <br />
* Ser A8 is angiotensinogen. <br />
* Ser A7 is a thyroxine-binding globulin.<br />
* Ser B1 is leukocyte elastase inhibitor<ref>PMID:26701651</ref>.<br />
* Ser B3 is squamos cell carcinoma antigen 1<ref>PMID:20527027</ref>. <br />
* Ser B5 is Maspin<ref>PMID:11309327</ref>.<br />
* Ser crmA is cysteine and serine proteinase inhibitor<ref>PMID:9065443</ref>.<br />
* Ser I1 is neuroserpin. <br />
* Ser A10 is protein Z-related protease inhibitor. <br />
* Ser A1 is [[Alpha-1-antitrypsin]]. <br />
* Ser A3 is α 1-antichymotrypsin.<br />
* Ser E1 is [[Plasminogen activator inhibitor]]. 


'''Serpin or serine protease inhibitor''' (Ser) are protease inhibitors.  Ser E1 is antithrombin.  Ser C1 is  antithrombin .  Ser A5 is protein C inhibitor.  Ser A6 is a cortisol-binding globulin.  Ser A8 is angiotensinogen.    Ser A7 is a thyroxine-binding globulin.  Ser B3 is squamos cell carcinoma antigen 1.  Ser I1 is neuroserpin. Ser A10 is protein Z-related protease inhibitor.  Ser A1 is alpha-1 antitrypsin.   Ser E1 is plasminogen activator inhibitor 1.
== Disease ==
Mutation in Ser A7 causes partial thyroxine-binding globulin deficiency<ref>PMID:24356794</ref>.  Ser B3 may contribute to tumor cell resistance to anti-neoplastic drugs<ref>PMID:25332258</ref>.  Ser A3 promotes growth of endometrial cancer cells <ref>PMID:24817931</ref>.
 
==Structural highlights ==
Ser A7 - a thyrosine-binding globulin - <scene name='51/517379/Cv/3'>binding site contains thyroxin derivative</scene><ref>PMID:21325280</ref>. Water molecules are shown as red spheres.  


==3D structures of serpin==
==3D structures of serpin==
[[Serpin 3D structures]]


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
</StructureSection>
 
===Ser===
 
[[1mtp]], [[1sng]] – Ser – ''Thermobifida fusca''
 
===Ser A1===
 
[[Alpha-1-antitrypsin]]
 
===Ser A5===
 
[[2ol2]] – hSer-A5<br />
[[3dy0]] – hSer-A5 + heparin
 
===Ser A6===
 
[[Corticosteroid-binding globulin]]
 
===Ser A7===
 
[[2riv]] – hSer-A7<br />
[[2riw]] – hSer-A7 + thyroxine<br />
[[2xn3]] – hSer-A7 + mefenamic acid<br />
[[2xn5]] – hSer-A7 + furosemide<br />
[[2xn6]], [[2xn7]] – hSer-A7 + thyroxine-fluoresein
 
===Ser A8===
 
[[2jp8]] – hSer-A8 – NMR<br />
[[2wxw]] – hSer-A8<br />
[[2x0b]] – hSer-A8 + renin<br />
[[2wxx]], [[2wxy]], [[2wy0]] – Ser-A8 – mouse<br />
[[2wxz]], [[2wy1]] – rSer-A8
 
===Ser A10===
 
[[3h5c]], [[3f1s]] – hSer-A10 + vitamin K-dependent protein Z


===Ser A12===
== References ==
 
<references/>  
[[4if8]] – hSer-A12<br />
 
===Ser B3===
 
[[2zv6]] – hSer-B3
 
===Ser C1===
 
[[Antithrombin]]
 
===Ser E1===
 
[[Plasminogen activator inhibitor]]
 
===Ser E2===
 
[[4dy0]] – hSer-E2 + heparin
 
===Ser-I1===
 
[[3fgq]], [[2f02]], [[3f5n]] – hSer-I1
 
===Ser K===
 
[[1sek]] – ThSer-K – Tobacco hornworm
 
===Ser 1===
 
[[1k9o]] – ThSer-1 (mutant) + trypsin II<br />
[[3le2]] – Ser-1 – ''Arabidopsis thaliana''
 
===Ser 2===
 
[[1m93]] – Ser-2 – Cowpox virus<br />
[[3nda]] – Ser-2 – Sheep tick<br />
[[3pzf]] – Ser-2 – malaria mosquito
 
===Maspin===
 
[[1xqg]], [[1xqj]], [[1wz9]], [[1xu8]] - hMapsin
 
 
 
</StructureSection>
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 14:45, 4 February 2020

Function

Serpin or serine protease inhibitor (Ser) are protease inhibitors.

Disease

Mutation in Ser A7 causes partial thyroxine-binding globulin deficiency[5]. Ser B3 may contribute to tumor cell resistance to anti-neoplastic drugs[6]. Ser A3 promotes growth of endometrial cancer cells [7].

Structural highlights

Ser A7 - a thyrosine-binding globulin - [8]. Water molecules are shown as red spheres.

3D structures of serpin

Serpin 3D structures


Structure of cleaved human serpin A7. Residues 32-380 (cyan), residues 381-415 (salmon) complex with thyroxine-fluoresein, ethylene glycol and Ca+2 ion (green) (PDB entry 2xn6)

Drag the structure with the mouse to rotate

ReferencesReferences

  1. ↑ El Ouaamari A, Dirice E, Gedeon N, Hu J, Zhou JY, Shirakawa J, Hou L, Goodman J, Karampelias C, Qiang G, Boucher J, Martinez R, Gritsenko MA, De Jesus DF, Kahraman S, Bhatt S, Smith RD, Beer HD, Jungtrakoon P, Gong Y, Goldfine AB, Liew CW, Doria A, Andersson O, Qian WJ, Remold-O'Donnell E, Kulkarni RN. SerpinB1 Promotes Pancreatic beta Cell Proliferation. Cell Metab. 2016 Jan 12;23(1):194-205. doi: 10.1016/j.cmet.2015.12.001. Epub 2015, Dec 15. PMID:26701651 doi:http://dx.doi.org/10.1016/j.cmet.2015.12.001
  2. ↑ Quarta S, Vidalino L, Turato C, Ruvoletto M, Calabrese F, Valente M, Cannito S, Fassina G, Parola M, Gatta A, Pontisso P. SERPINB3 induces epithelial-mesenchymal transition. J Pathol. 2010 Jul;221(3):343-56. doi: 10.1002/path.2708. PMID:20527027 doi:http://dx.doi.org/10.1002/path.2708
  3. ↑ Maass N, Hojo T, Ueding M, Luttges J, Kloppel G, Jonat W, Nagasaki K. Expression of the tumor suppressor gene Maspin in human pancreatic cancers. Clin Cancer Res. 2001 Apr;7(4):812-7. PMID:11309327
  4. ↑ Zhou Q, Snipas S, Orth K, Muzio M, Dixit VM, Salvesen GS. Target protease specificity of the viral serpin CrmA. Analysis of five caspases. J Biol Chem. 1997 Mar 21;272(12):7797-800. PMID:9065443
  5. ↑ Sklate RT, Olcese MC, Maccallini GC, Sarmiento RG, Targovnik HM, Rivolta CM. Novel mutation p.A64D in the Serpina7 gene as a cause of partial thyroxine-binding globulin deficiency associated with increases affinity in transthyretin by a known p.A109T mutation in the TTR gene. Horm Metab Res. 2014 Feb;46(2):100-8. doi: 10.1055/s-0033-1358741. Epub 2013 Dec , 19. PMID:24356794 doi:http://dx.doi.org/10.1055/s-0033-1358741
  6. ↑ Pontisso P. Role of SERPINB3 in hepatocellular carcinoma. Ann Hepatol. 2014 Nov-Dec;13(6):722-7. PMID:25332258
  7. ↑ Yang GD, Yang XM, Lu H, Ren Y, Ma MZ, Zhu LY, Wang JH, Song WW, Zhang WM, Zhang R, Zhang ZG. SERPINA3 promotes endometrial cancer cells growth by regulating G2/M cell cycle checkpoint and apoptosis. Int J Clin Exp Pathol. 2014 Mar 15;7(4):1348-58. eCollection 2014. PMID:24817931
  8. ↑ Qi X, Loiseau F, Chan WL, Yan Y, Wei Z, Milroy LG, Myers RM, Ley SV, Read RJ, Carrell RW, Zhou A. Allosteric modulation of hormone release from thyroxine and corticosteroid binding-globulins. J Biol Chem. 2011 Feb 16. PMID:21325280 doi:10.1074/jbc.M110.171082

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Michal Harel, Alexander Berchansky
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